| EC |
4.1.1.85 |
| Accepted name: |
3-dehydro-L-gulonate-6-phosphate decarboxylase |
| Reaction: |
3-dehydro-L-gulonate 6-phosphate + H+ = L-xylulose 5-phosphate + CO2 |
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For diagram of the bacterial pathway of ascorbic-acid catabolism, click here |
| Other name(s): |
3-keto-L-gulonate 6-phosphate decarboxylase; UlaD; SgaH; SgbH; KGPDC; 3-dehydro-L-gulonate-6-phosphate carboxy-lyase |
| Systematic name: |
3-dehydro-L-gulonate-6-phosphate carboxy-lyase (L-xylulose-5-phosphate-forming) |
| Comments: |
Requires Mg2+. Along with EC 5.1.3.22, L-ribulose-5-phosphate 3-epimerase, this enzyme is involved in a pathway for the utilization of L-ascorbate by Escherichia coli. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Yew, W.S. and Gerlt, J.A. Utilization of L-ascorbate by Escherichia coli K-12: assignments of functions to products of the yjf-sga and yia-sgb operons. J. Bacteriol. 184 (2002) 302–306. [DOI] [PMID: 11741871] |
| 2. |
Wise, E., Yew, W.S., Babbitt, P.C., Gerlt, J.A. and Rayment, I. Homologous 8-barrel enzymes that catalyze unrelated reactions: orotidine 5′-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry 41 (2002) 3861–3869. [DOI] [PMID: 11900527] |
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| [EC 4.1.1.85 created 2005] |
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